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Original

Aspects of preanalytical variation of lactoferrin and elastase/α1-protease inhibitor complexes

, &
Pages 263-274 | Received 28 Jul 1992, Accepted 07 Dec 1992, Published online: 29 Mar 2011

References

  • Dewald B, Rindler-Ludwig R, Bretz U, Baggioneli M. Subcellular localization and heterogeneity of neutral proteases in neutrophilic polymorphonuclear leukocytes. J Exp Med 1975; 141: 709–23
  • Spitznagel J K, Dalldorf F G, Leffell M S. Character of azurophil and specific granules purified from human polymorphonuclear leucocytes. Lab Invest 1974; 30: 774–85
  • Miyauchi J, Watanabe Y. Immunocytochemical localization of lactoferrin in human neutrophils. An ultrastructural and morphometrical study. Cell Tissue Res 1987; 247: 249–58
  • Masson P L, Heremans J F, Dive C. An iron-binding protein common to many external secretions. Clin Chim Acta 1966; 14: 735–9
  • Senior R M, Campbell E J, Landis J A, Cox F R, Kuhn C, Koren C, Koren H S. Elastase of U-937 monocytelike cells. Comparisons with elastases derived from human monocytes and neutrophils and murine macrophagelike cells. J Clin Invest 1982; 69: 384–93
  • Bristow C L, Lyford L K, Stevens D P, Flood P M. Elastase is a constituent product of T cells. Bio-chem Biophys Res Com 1991; 181: 232–9
  • Lungarella G, Menegazzi R, Gardi C, Spessotto P, deSanti M M, Bertoncin P, Patriarca P, Calzoni P, Zabucchi G. Identification of elastase in human eosinophils: Immunolocalization, isolation and partial characterization. Arch Biochem Biophys 1992; 292: 128–35
  • Ohlsson K, Olsson I. Neutral proteases of human granulocytes. HI. Interaction between human granulocyte elastase and plasma protease inhibitors. Scand J Clin Lab Invest 1974; 34: 349–55
  • Adeyemi E O, Hodgson H JF. Molecular distribution of elastase between its two main inhibitors: direct quantitation of elastase-α2-macroglobulin complex with a novel ELISA technique. Scand J Clin Lab Invest 1990; 50: 433–40
  • Browser M S, Harpel P C. Alpha-1-antitrypsin-Human Leukocyte elastase complexes in blood: Quantification by an enzyme-linked differential antibody immunosorbent assay and comparison with alpha-2-plasmin inhibitor-plasmin complexes. Blood 1983; 16: 842–9
  • Neumann S, Gunzer G, Hennrich N, Lang H. Enzyme immunoassay for human polymorphonuclear elastase complexed with alfa-1-proteinase inhibitor. J Clin Chem Clin Biochem 1984; 22: 693–7
  • Boger C, Yuan H Z, Schultek T, Tegtmeier K-F, Wood W G. Development and clinical evaluation of immunoluminometric assays for lactoferrin and elastase-a i-proteinase inhibitor complexes in body fluids with special references to bronchoalveolar lavage and neonatal sepsis. J Clin Chem Clin Biochem. 1988; 26: 645–51
  • Kramer M D, Muller-Bardorff M, Simon M M, Tilgen W, Schickel E, Petzoldt D. Measurement of free human leukocyte elastase and human leukocyte elastase/α1-proteinase inhibitor complexes by an enzyme-linked immunosorbent assay. J Immun Methods 1990; 131: 41–8
  • Hamaguchi Y, Suzumura H, Taya M, Sakakura Y. ELISA for determination of immunoreactive free elastase and elastase in complex with α1,-antitrypsin in nasal secretions with sinuitis. Acta Otolaryngol 1991; 111: 542–9
  • Antonsen S, Wanscher M. An ELISA for elastase/ α1-protease inhibitor complexes in human plasma and serum. Scand J Clin Lab Invest 1993; 53: 145–153
  • Hansen N E, Karle H, Andersen V, Malmquist J, Hoff G E. Neutrophilic granulocytes in bacterial infection. Sequential studies on lysozyme, myeloperoxidase and lactoferrin. Clin Exp Immunol 1976; 26: 463–8
  • Venge P, Stromberg A, Braconier J H, Roxin L-e, Olsson I. Neutrophil and eosinophil granulocytes in bacterial infection: Sequential studies of cellular and serum levels of granule proteins. Br J Haema-tology 1978; 38: 475–83
  • Duswald K H. Zur Pathobiochemie der Leukozyten-Elastase und ausgewählter Plasmaproteine bei Sepsis nach abdominalchirurgischen Eingriffen. G.I.T. Verlag, Darmstadt, West-Germany 1983
  • Baynes R, Bezwoda W, Bothwell T, Khan Q, Man-Soor N. The non-immune inflammatory response: Serial changes in plasma iron, iron-binding capacity, lactoferrin, ferritin and C-reactive protein. Scand J Clin Lab Invest 1986; 46: 695–704
  • Speer C P, Ninjo A, Gahr M. Elastase-α1-proteinase inhibitor in early diagnosis of neonatal septicemia. J Pediatrics 1986; 108: 987–90
  • Seitz R, Wolff M, Egbring R, Radtke K P, Liesen-Feld A, Pittner P, Havemann K. Participation and interactions of neutrophil elastase in haemostatic disorders of patients with severe infections. Eur J Haematol 1987; 38: 231–40
  • Scott P H. Plasma lactoferrin levels in newborn preterm infants: effects of infection. Ann Clin Biochem 1989; 26: 412–5
  • Tsaka T, Herkner K R. Polymorphonuclear elastase in neonatal sepsis. Clin Chim Acta 1990; 193: 103–12
  • Lasson Å, Balldin G, Ohlsson K. Leucocyte elastase α1-proteinase inhibitor complexes may diagnose pancreatic absceses early. Scand J Gastroenterol 1986; 21: 221–4
  • Gross V, Schölmerich J, Leser H G, Salm R, Lau-Sen M, Rückauer K, Schöffel U, Lay L, Heinisch A, Farthmann E H, Gerok W. Granulocyte elastase in assessment of severity of acute pancreatitis. Comparison with acute-phase proteins C-reactive protein, a [-antitrypsin, and protease inhibitor ai-macroglobulin. Dig Dis Sci 1990; 35: 97–105
  • Uhl W, Büchler M, Malfertheimer P, Martini M, Beger H G. PMN-elastase in comparison with CRP, antiproteases and LDH as indicators of necrosis in human acute pancreatitis. Pancreas 1991; 6: 253–9
  • Adeyemi E O, Neumann S, Chadwick V S, Hodgson H JF, Pepys M B. Circulating human leucocyte elastase in patients with inflammatory bowel disease. Gut 1985; 26: 1306–11
  • Fink P C, Suin de BoutemardHaeckel R, Welmann W. Endotoxaemia in patients with Crohn's disease: A longitudinal study of elastase-proteinase inhibitor and limulus-amoebocyte-lysate reactivity. J Clin Chem Clin Biochem 1988; 26: 117–22
  • Wolach B, Coates T D, Hugli T E, Baehner R L, Boxer L A. Plasma lactoferrin reflects granulocyte activation via complement in burn patients. J lab Clin Med 1984; 103: 284–93
  • Barisoni D, Bellavite P, Bonazzi M L, Zermani R, Bortolani A. Monitoring of elastase in plasma of burned patients in relation to other inflammation parameters. Burns 1991; 17: 141–6
  • Schnebli H P, Christen P, Jochum M, Mallya R K, Pepys M B. Plasma levels of inhibitor-bound leukocytic elastase in rheumatoid arthritis patients. Proteases-Potential Role in Health and Disease, W H Hörl, A Heidland. Plenum Press, New York 1984; 355–62
  • Adeyemi E O, Campos L B, Loizou S, Walport M J, Hodgson H JF. Plasma lactoferrin and neutrophil elastase in rheumatoid arthritis and systemic lupus erythematosus. Br J Rheumatol 1990; 29: 15–20
  • Kuramitsu K, Yoshida A. Plasma and synovial fluid levels of granulocytal elastase-α1-1-protease inhibitor complex in patients with rheumatoid arthritis. Rheumatol Int 1990; 10: 51–6
  • Feltelius N, Hallgren R. Circulating inhibitor bound elastase in patients with ankylosing spondylitis and rheumatoid arthritis and the influence of sulphasalazine treatment. Ann Rheum Dis 1988; 47: 10–4
  • Banks R E, Evans S W, Taylor K F, Bird H A, Whicher J T. Measurement of plasma concentrations of polymorphonuclear elastase-α1 proteinase inhibitor (elastase-al antitrypsin) in patients with rheumatoid arthritis: interference by rheumatoid factor. Annals Rheum Dis 1990; 49: 18–21
  • MørkHansen T, Hansen N E, Birgens H S, H0lund B, Lorenzen I. Serum ferritin and the assessment of iron deficiency in rheumatoid arthritis. Scand J Rheumatol 1983; 12: 353–9
  • Hällgren R, Venge P. Hemodialysis-induced increase in serum lactoferrin and serum eosinophil cationic protein as signs of local neutrophil and eosinophil degranulation. Nephron 1981; 29: 233–38
  • Knudsen F, Nielsen A H, Pedersen J D. Leukopenia and release of granulocyte elastase: Interlinked membrane-dependent events during hemodialysis. Blood Purification 1984; 2: 36–40
  • Antonsen S, Brandslund I, Clemensen S, S0feldt S, Madsen T, Alstrup P. Neutrophil lysosomal enzyme release and complement activation during cardiopulmonary bypass. Scand J Thor Cardiovasc Surg 1987; 21: 47–52
  • Venge P, Nilsson L, Nystrom S-O, Aberg T. Serum and plasma measurements of neutrophil granule proteins during cardiopulmonary bypass: A model to estimate human turnover of lactoferrin and myeloperoxidase. Eur J Haematol 1987; 39: 339–45
  • Wachtfogel Y T, Kucich U, Greenplate J, Gluszko P, Abrams W, Weinbaum G, Wenger R K, Rucins-Ki B, Niewiarowski S, Edmunds L H, Colman R W. Human neutrophil degranulation during extracorporeal circulation. Blood 1987; 69: 324–30
  • Wanscher M, Knudsen F, Antonsen S, Hansen S H. Release of granulocyte elastase and complement changes during hysterectomy. Scand J Clin Lab Invest 1989; 49: 255–8
  • Wanscher M, Antonsen S, Toft P, Knudsen F, Helbo-Hansen H S. Attenuation of intraoperative surgical stress response has no influence on postoperative degranulation of polymorphonuclear granulocytes. Eur J Anaestesiology 1991; 8: 393–400
  • Olofsson T, Olsson I, Venge P, Elgefors B. Serum myeloperoxidase and lactoferrin in neutropenia. Scand J Haematol 1977; 18: 73–80
  • Birgens H S. Lactoferrin plasma measured by an ELISA technique: Evidence that plasma lactoferrin is an indicator of neutrophil turnover and bone marrow activity in acute leukaemia. Scand J Haematol 1985; 34: 326–31
  • Baynes R D, Bezwoda W R, Khan Q, Mansoor N. Relationship of plasma lactoferrin content to neutrophil regeneration and bone marrow infusion. Scand J Haematol 1986; 36: 79–84
  • Baynes R D, Bezwoda W R, Khan Q, Mansoor N. Plasma lactoferrin content: Differential effect of steroid administration and infective illnesses: Lack
  • Boxer L A, Coates T D, Haak R A, Wolach J B, Hoffstein S, Baehner R L. Lactoferrin deficiency associated with altered granulocyte function. New Eng J Med 1982; 307: 404–10
  • Dufax B, Order U. Plasma elastase-α1 -antitrypsin, neopterin, tumor necrosis factor and soluble inter-leukin-2 receptor after prolonged exercise. Int J Sports Med 1989; 10: 434–8
  • Adeyemi E O, Hodgson H JF. Augmented release of human leucocyte lactoferrin (and elastase) during coagulation. J Clin Lab Immunol 1988; 27: 1–4
  • Olsson I, Olofsson T, Ohlsson K, Gustavson A. Serum and plasma myeloperoxidase, elastase and lactoferrin content in acute myeloid leukaemia. Scand J Haematol 1979; 22: 397–406
  • Barthe C, Galabert C, Guy-Crotte O, Figarella C. Plasma and serum lactoferrin levels in cystic fibrosis. Relationship with the presence of cystic fibrosis protein 1989; 181: 183–8
  • Bennet R M, Mohla C. A solid-phase radioimmunoassay for the measurement of lactoferrin in human plasma: Variations with age, sex and disease. J Lab Clin Med 1976; 88: 156–66
  • Broxmeyer H E, Gentile P, Bognacki J, Ralph P. Lactoferrin, transferrin and acidic isoferritins: Regulatory molecules with potential therapeutic value in leukaemia. Blood Cells 1983; 9: 83–105
  • Otnaess A BK, Meberg A, Sande H A. Plasma lactoferrin measured by an enzyme-linked immunosorbent assay (ELISA). Measurements on adult and infant plasma. Scand J Haematol 1983; 31: 235–40
  • Antonsen S, Wiggers P, Dalhej J, Blaabjerg O. An enzyme-linked immunosorbent assay for plasma-lactoferrin. Concentrations in 362 healthy, adult blood donors. Scand J Clin Lab Invest 1993; 53: 133–144
  • Bliss C I. Statistics in Biology. McGraw-Hill, New York 1967
  • Wright D G. The neutrophil as a secretory organ of host defense. Advances in host defense mechanisms, J I Gallin, A S Fauci. Raven Press, New York 1982; 75–110

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